大戟乳胶中一种凝集素的纯化及部分特性分析
Purification and partial characterization of a lectin from Euphorbia neriifolia latex.
作者信息
Seshagirirao K, Prasad M N
机构信息
Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India.
出版信息
Biochem Mol Biol Int. 1995 May;35(6):1199-204.
A lectin was purified from Euphorbia neriifolia latex to homogeneity by affinity chromatography on Sepharose 4B. The protein appears to be a dimer with approximate M(r) of 60,000 on gel filtration and showing a single band at M(r) 32,000 in SDS-PAGE, and contains 12.3% carbohydrate. It agglutinated trypsinized human and rabbit erythrocytes, but not sheep erythrocytes. However, sialidase-treated sheep erythrocytes were agglutinated. The galactose and galactose containing sugars inhibited the heamagglutination with increased beta-anomeric specificity. The Euphorbia lectin possesses mitogenic activity with murine spleen lymphocytes but it does not inhibit protein synthesis in rabbit reticulocyte lysate.
通过在琼脂糖4B上进行亲和层析，从大戟科麻风树胶乳中纯化出一种凝集素，使其达到同质。该蛋白质在凝胶过滤中似乎是一种近似分子量为60,000的二聚体，在SDS-PAGE中显示出一条分子量为32,000的单带，并且含有12.3%的碳水化合物。它能凝集经胰蛋白酶处理的人和兔红细胞，但不能凝集绵羊红细胞。然而，经唾液酸酶处理的绵羊红细胞可被凝集。含半乳糖和半乳糖的糖类以增加的β-异头物特异性抑制血凝。大戟凝集素对小鼠脾淋巴细胞具有促有丝分裂活性，但它不抑制兔网织红细胞裂解物中的蛋白质合成。
Zotero 插件